Bard1 (BRCA1 associated RING domain 1) encodes a protein that interacts with the N-terminal region of BRCA1 and has homology with the 2 most conserved regions of BRCA1, the N-terminal RING motif and the C-terminal BRCT domain. The BARD1/BRCA1 interaction is implicated in tumor suppression. Mutations in BARD1 are associated with breast cancer and hereditary breast ovarian cancer syndrome. 
 Bard1-D488H knock-in mice express a D488H (aspartic acid to histidine) amino acid substitution. The mutation corresponds to human tumor-associated missense mutations in the ankyrin domain that disrupts BARD1 recognition of H4K20me0 (histone H4 unmethylated at lysine 20). Mice heterozygous for the mutation are viable and fertile. Embryos homozygous for the mutation are not viable. This strain may be useful in studies of tumor suppression and breast cancer.

Bard1-D488H knock-in mice express a D488H (aspartic acid to histidine) amino acid substitution in the Bard1 (BRCA1 associated RING domain 1) locus. The D488H mutation is homozygous embryonic lethal. This strain may be useful in studies of tumor suppression and breast cancer.

This strain is hosted by NIH's MMRRC, which partners with JAX for the distribution of this and other strains. For additional information and to purchase, please visit the MMRRC site.